메뉴 건너뛰기




Volumn 143, Issue 1, 2008, Pages 49-57

D-serine dehydratase from chicken kidney: A vertebral homologue of the cryptic enzyme from Burkholderia cepacia

Author keywords

Chicken kidney; D serine; D serine dehydratase; Proximal tubules; Pyridoxal 5 phosphate

Indexed keywords

AMINOOXYACETIC ACID; COMPLEMENTARY DNA; DEXTRO SERINE; FRUCTOSE BISPHOSPHATE ALDOLASE; HETERODIMER; HYDROLYASE; HYDROXYLAMINE; PYRIDOXAL 5 PHOSPHATE; SERINE; THREONINE;

EID: 38849177419     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvm203     Document Type: Article
Times cited : (26)

References (40)
  • 2
    • 0027976595 scopus 로고
    • Distribution of free D-serine in vertebrate brains
    • Nagata, Y., Horiike, K., and Maeda, T. (1994) Distribution of free D-serine in vertebrate brains. Brain Res. 634, 291-295
    • (1994) Brain Res , vol.634 , pp. 291-295
    • Nagata, Y.1    Horiike, K.2    Maeda, T.3
  • 4
    • 0033539510 scopus 로고    scopus 로고
    • Serine racemase: A glial enzyme synthesizing D-serine to regulate glutamate-N-methyl-D-aspartate neurotransmission
    • Wolosker, H., Blackshaw, S., and Snyder, S.H. (1999) Serine racemase: a glial enzyme synthesizing D-serine to regulate glutamate-N-methyl-D-aspartate neurotransmission. Proc. Natl Acad. Sci. USA 96, 13409-13414
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 13409-13414
    • Wolosker, H.1    Blackshaw, S.2    Snyder, S.H.3
  • 5
    • 0028176862 scopus 로고    scopus 로고
    • Horiike, K., Tojo, H., Arai, R., Nozaki, M., and Maeda, T. (1994) D-Amino-acid oxidase is confined to the lower brain stem and cerebellum in rat brain: regional differentiation of astrocytes. Brain Res. 652, 297-303
    • Horiike, K., Tojo, H., Arai, R., Nozaki, M., and Maeda, T. (1994) D-Amino-acid oxidase is confined to the lower brain stem and cerebellum in rat brain: regional differentiation of astrocytes. Brain Res. 652, 297-303
  • 6
    • 0028988978 scopus 로고    scopus 로고
    • Schell, M.J., Molliver, M.E., and Snyder, S.H. (1995) D-Serine, an endogenous synaptic modulator: localization to astrocytes and glutamate-stimulated release. Proc. Natl Acad. Sci. USA 92, 3948-3952
    • Schell, M.J., Molliver, M.E., and Snyder, S.H. (1995) D-Serine, an endogenous synaptic modulator: localization to astrocytes and glutamate-stimulated release. Proc. Natl Acad. Sci. USA 92, 3948-3952
  • 7
    • 0035961626 scopus 로고    scopus 로고
    • Distribution of D-amino-acid oxidase and D-serine in vertebrate brains
    • Horiike, K., Ishida, T, Tanaka, H., and Arai, R. (2001) Distribution of D-amino-acid oxidase and D-serine in vertebrate brains. J. Mol. Catal. 12B, 37-41
    • (2001) J. Mol. Catal , vol.12 B , pp. 37-41
    • Horiike, K.1    Ishida, T.2    Tanaka, H.3    Arai, R.4
  • 8
    • 2942718893 scopus 로고    scopus 로고
    • The N-methyl D-aspartate receptor glycine site and D-serine metabolism: An evolutionary perspective
    • Schell, M.J. (2004) The N-methyl D-aspartate receptor glycine site and D-serine metabolism: an evolutionary perspective. Phil. Trans. R. Soc. Lond. B 359, 943-964
    • (2004) Phil. Trans. R. Soc. Lond. B , vol.359 , pp. 943-964
    • Schell, M.J.1
  • 10
    • 0037195093 scopus 로고    scopus 로고
    • Cofactors of serine racemase that physiologically stimulate the synthesis of the N-methyl-L-aspartate (NMDA) receptor coagonist D-serine
    • de Miranda, J., Panizzutti, R., Foltyn, V.N., and Wolosker, H. (2002) Cofactors of serine racemase that physiologically stimulate the synthesis of the N-methyl-L-aspartate (NMDA) receptor coagonist D-serine. Proc. Natl Acad. Sci. USA 99, 14542-14547
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 14542-14547
    • de Miranda, J.1    Panizzutti, R.2    Foltyn, V.N.3    Wolosker, H.4
  • 13
    • 85019441826 scopus 로고    scopus 로고
    • Mustafa, A.K., Kim, P.M., and Snyder, S.H. (2004) D-Serine as a putative glial neurotransmitter. Neuron Glia Biol. 1, 275-281
    • Mustafa, A.K., Kim, P.M., and Snyder, S.H. (2004) D-Serine as a putative glial neurotransmitter. Neuron Glia Biol. 1, 275-281
  • 14
    • 20544462810 scopus 로고    scopus 로고
    • Fuchs, S.A., Berger, R., Klomp, L.W.J., and de Koning, T.J. (2005) D-Amino acids in the central nervous system in health and disease. Mol. Genet. Metab. 85, 168-180
    • Fuchs, S.A., Berger, R., Klomp, L.W.J., and de Koning, T.J. (2005) D-Amino acids in the central nervous system in health and disease. Mol. Genet. Metab. 85, 168-180
  • 15
    • 24944443321 scopus 로고    scopus 로고
    • Metabolism and functional roles of endogenous D-serine in mammalian brains
    • Nishikawa, T. (2005) Metabolism and functional roles of endogenous D-serine in mammalian brains. Biol. Pharm. Bull. 28, 1561-1565
    • (2005) Biol. Pharm. Bull , vol.28 , pp. 1561-1565
    • Nishikawa, T.1
  • 16
    • 33645027023 scopus 로고    scopus 로고
    • Gliotransmission at central glutamatergic synapses: D-serine on stage
    • Martineau, M., Baux, G., and Mothet, J.-P. (2006) Gliotransmission at central glutamatergic synapses: D-serine on stage. J. Physiol. Paris 99, 103-110
    • (2006) J. Physiol. Paris , vol.99 , pp. 103-110
    • Martineau, M.1    Baux, G.2    Mothet, J.-P.3
  • 17
    • 33746362592 scopus 로고    scopus 로고
    • Martineau, M., Baux, G., and Mothet, J.-P. (2006) D-Serine signaling in the brain: friend and foe. Trends Neurosci. 29, 481-491
    • Martineau, M., Baux, G., and Mothet, J.-P. (2006) D-Serine signaling in the brain: friend and foe. Trends Neurosci. 29, 481-491
  • 18
    • 36448987536 scopus 로고    scopus 로고
    • Scolari, M.J. and Acosta, G.B. (2007) D-Serine: a new word in the glutamatergic neuro-glial language. Amino Acids (in press, doi: 10.1007)
    • Scolari, M.J. and Acosta, G.B. (2007) D-Serine: a new word in the glutamatergic neuro-glial language. Amino Acids (in press, doi: 10.1007)
  • 19
    • 0038037859 scopus 로고    scopus 로고
    • Mechanisms of activation, inhibition and specificity: Crystal structures of the NMDA receptor NR1 ligand-binding core
    • Furukawa, H. and Gouaux, E. (2003) Mechanisms of activation, inhibition and specificity: crystal structures of the NMDA receptor NR1 ligand-binding core. EMBO J. 22, 2873-2885
    • (2003) EMBO J , vol.22 , pp. 2873-2885
    • Furukawa, H.1    Gouaux, E.2
  • 20
    • 0013855897 scopus 로고    scopus 로고
    • Grillo, M.A., Fossa, T., and Coghe, M. (1965) D-Serine dehydratase of chicken kidney. Enzymologia 28, 377-388
    • Grillo, M.A., Fossa, T., and Coghe, M. (1965) D-Serine dehydratase of chicken kidney. Enzymologia 28, 377-388
  • 21
    • 33846655347 scopus 로고    scopus 로고
    • Simultaneous measurement of D-serine dehydratase and D-amino acid oxidase activities by the detection of 2-oxo-acid formation with reverse-phase high-performance liquid chromatography
    • Tanaka, H., Yamamoto, A., Ishida, T., and Horiike, K. (2007) Simultaneous measurement of D-serine dehydratase and D-amino acid oxidase activities by the detection of 2-oxo-acid formation with reverse-phase high-performance liquid chromatography. Anal. Biochem. 362, 83-88
    • (2007) Anal. Biochem , vol.362 , pp. 83-88
    • Tanaka, H.1    Yamamoto, A.2    Ishida, T.3    Horiike, K.4
  • 22
    • 0023771138 scopus 로고    scopus 로고
    • Marceau, M., McFall, E., Lewis, S.D., and Shafer, J.A. (1988) D-Serine dehydratase from Escherichia coli. DNA sequence and identification of catalytically inactive glycine to aspartic acid variants. J. Biol. Chem. 263, 16926-16933
    • Marceau, M., McFall, E., Lewis, S.D., and Shafer, J.A. (1988) D-Serine dehydratase from Escherichia coli. DNA sequence and identification of catalytically inactive glycine to aspartic acid variants. J. Biol. Chem. 263, 16926-16933
  • 23
    • 0019120834 scopus 로고
    • Hydroxyamino acid utilization and α-ketobutyrate toxicity in Pseudomonas cepacia
    • Wong, H.C., Allenza, P., and Lessie, T.G. (1980) Hydroxyamino acid utilization and α-ketobutyrate toxicity in Pseudomonas cepacia. J. Bacteriol. 144, 441-443
    • (1980) J. Bacteriol , vol.144 , pp. 441-443
    • Wong, H.C.1    Allenza, P.2    Lessie, T.G.3
  • 24
    • 0032479296 scopus 로고    scopus 로고
    • A novel metal-activated pyridoxal enzyme with a unique primary structure, low specificity D-threonine aldolase from Arthrobacter sp. strain DK-38. Molecular cloning and cofactor characterization
    • Liu, J.-Q., Dairi, T., Itoh, N., Kataoka, M., Shimizu, S., and Yamada, H. (1998) A novel metal-activated pyridoxal enzyme with a unique primary structure, low specificity D-threonine aldolase from Arthrobacter sp. strain DK-38. Molecular cloning and cofactor characterization. J. Biol. Chem. 273, 16678-16685
    • (1998) J. Biol. Chem , vol.273 , pp. 16678-16685
    • Liu, J.-Q.1    Dairi, T.2    Itoh, N.3    Kataoka, M.4    Shimizu, S.5    Yamada, H.6
  • 25
    • 0013892496 scopus 로고
    • Distribution of D-amino acid oxidase in bovine and human nervous tissues
    • Neims, A.H., Zieverink, W.D., and Smilack, J.D. (1966) Distribution of D-amino acid oxidase in bovine and human nervous tissues. J. Neurochem. 13, 163-168
    • (1966) J. Neurochem , vol.13 , pp. 163-168
    • Neims, A.H.1    Zieverink, W.D.2    Smilack, J.D.3
  • 26
    • 34248647913 scopus 로고    scopus 로고
    • Functional and structural characterization of D-aspartate oxidase from porcine kidney: Non-Michaelis kinetics due to substrate activation
    • Yamamoto, A., Tanaka, H., Ishida, T., and Horiike, K. (2007) Functional and structural characterization of D-aspartate oxidase from porcine kidney: non-Michaelis kinetics due to substrate activation. J. Biochem. 141, 363-376
    • (2007) J. Biochem , vol.141 , pp. 363-376
    • Yamamoto, A.1    Tanaka, H.2    Ishida, T.3    Horiike, K.4
  • 27
    • 0026455011 scopus 로고
    • Determination of free amino acid enantiomers in rat brain and serum by high-performance liquid chromatography after derivatization with N-tert-butyloxycarbonyl-L-cysteine and o-phthaldialdehyde
    • Hashimoto, A., Nishikawa, T., Oka, T., Takahashi, K., and Hayashi, T. (1992) Determination of free amino acid enantiomers in rat brain and serum by high-performance liquid chromatography after derivatization with N-tert-butyloxycarbonyl-L-cysteine and o-phthaldialdehyde. J. Chromatogr. 582, 41-48
    • (1992) J. Chromatogr , vol.582 , pp. 41-48
    • Hashimoto, A.1    Nishikawa, T.2    Oka, T.3    Takahashi, K.4    Hayashi, T.5
  • 28
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0026694947 scopus 로고
    • In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional gel electrophoresis
    • Rosenfeld, J., Capdevielle, J., Guillemot, J.C., and Ferrara, P. (1992) In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional gel electrophoresis. Anal. Biochem. 203, 173-179
    • (1992) Anal. Biochem , vol.203 , pp. 173-179
    • Rosenfeld, J.1    Capdevielle, J.2    Guillemot, J.C.3    Ferrara, P.4
  • 31
    • 0025129066 scopus 로고
    • Internal amino acid sequencing of proteins by in situ cyanogen bromide cleavage in polyacrylamide gels
    • Jahnen, W., Ward, L.D., Reid, G.E., Moritz, R.L., and Simpson, R.J. (1990) Internal amino acid sequencing of proteins by in situ cyanogen bromide cleavage in polyacrylamide gels. Biochem. Biophys. Res. Commun. 166, 139-145
    • (1990) Biochem. Biophys. Res. Commun , vol.166 , pp. 139-145
    • Jahnen, W.1    Ward, L.D.2    Reid, G.E.3    Moritz, R.L.4    Simpson, R.J.5
  • 32
    • 0024321837 scopus 로고    scopus 로고
    • Hayashi, Y., Matsui, H., and Takagi, T. (1989) Membrane protein molecular weight determined by low-angle laser light scattering photometry coupled with high-performance gel chromatography in Methods in Enzymology (Fleischer, S. and Fleischer, B., eds.) 172, pp. 514-528 Academic Press, San Diego
    • Hayashi, Y., Matsui, H., and Takagi, T. (1989) Membrane protein molecular weight determined by low-angle laser light scattering photometry coupled with high-performance gel chromatography in Methods in Enzymology (Fleischer, S. and Fleischer, B., eds.) Vol. 172, pp. 514-528 Academic Press, San Diego
  • 33
    • 0028988356 scopus 로고
    • Overexpression of Pseudomonas putida catechol 2,3-dioxygenase with high specific activity by genetically engineered Escherichia coli
    • Kobayashi, T., Ishida, T., Horiike, K., Takahara, Y., Numao, N., Nakazawa, A., Nakazawa, T., and Nozaki, M. (1995) Overexpression of Pseudomonas putida catechol 2,3-dioxygenase with high specific activity by genetically engineered Escherichia coli. J. Biochem. 117, 614-622
    • (1995) J. Biochem , vol.117 , pp. 614-622
    • Kobayashi, T.1    Ishida, T.2    Horiike, K.3    Takahara, Y.4    Numao, N.5    Nakazawa, A.6    Nakazawa, T.7    Nozaki, M.8
  • 35
    • 0035895311 scopus 로고    scopus 로고
    • Identification of lysine 346 as a functionally important residue for pyridoxal 5′-phosphate binding and catalysis in lysine 2,3-aminomutase from Bacillus subtilis
    • Chen, D. and Frey, P.A. (2001) Identification of lysine 346 as a functionally important residue for pyridoxal 5′-phosphate binding and catalysis in lysine 2,3-aminomutase from Bacillus subtilis. Biochemistry 40, 596-602
    • (2001) Biochemistry , vol.40 , pp. 596-602
    • Chen, D.1    Frey, P.A.2
  • 36
    • 0001515809 scopus 로고
    • The enzymatic oxidation of pyridoxine and pyridoxamine phosphates
    • Wada, H. and Snell, E.E. (1961) The enzymatic oxidation of pyridoxine and pyridoxamine phosphates. J. Biol. Chem. 236, 2089-2095
    • (1961) J. Biol. Chem , vol.236 , pp. 2089-2095
    • Wada, H.1    Snell, E.E.2
  • 37
    • 14144252024 scopus 로고    scopus 로고
    • Crystal structure of the pyridoxal-5′-phosphate-dependent serine dehydratase from human liver
    • Sun, L., Bartlam, M., Liu, Y., Pang, H., and Rao, Z. (2005) Crystal structure of the pyridoxal-5′-phosphate-dependent serine dehydratase from human liver. Protein Sci. 14, 791-798
    • (2005) Protein Sci , vol.14 , pp. 791-798
    • Sun, L.1    Bartlam, M.2    Liu, Y.3    Pang, H.4    Rao, Z.5
  • 39
    • 0001388651 scopus 로고
    • Histochemical staining of cells containing flavoenzyme D-amino acid oxidase based on its enzymatic activity: Application of a coupled peroxidation method
    • Horiike, K., Arai, R., Tojo, H., Yamano, T., Nozaki, M., and Maeda, T. (1985) Histochemical staining of cells containing flavoenzyme D-amino acid oxidase based on its enzymatic activity: application of a coupled peroxidation method. Acta Histochem. Cytochem. 18, 539-550
    • (1985) Acta Histochem. Cytochem , vol.18 , pp. 539-550
    • Horiike, K.1    Arai, R.2    Tojo, H.3    Yamano, T.4    Nozaki, M.5    Maeda, T.6
  • 40
    • 0033067656 scopus 로고    scopus 로고
    • Silbernagl, S., Völker, K., and Dantzler, W.H. (1999) D-Serine is reabsorbed in rat renal pars recta. Am. J. Physiol. 276, F857-F863
    • Silbernagl, S., Völker, K., and Dantzler, W.H. (1999) D-Serine is reabsorbed in rat renal pars recta. Am. J. Physiol. 276, F857-F863


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.